Filamin inhibits actomyosin ATPase activity in platelet |
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| Authors: | T Onji M Takagi N Shibata |
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| Affiliation: | 1. Department of Pharmacology, University of Michigan Medical School, Ann Arbor, MI, United States of America;2. Department of Internal Medicine, Division of Cardiovascular Medicine, University of Michigan Medical School, Ann Arbor, MI, United States of America;1. Laboratory of Angiopathology, Institute of General Pathology and Pathophysiology, Russian Academy of Medical Sciences, Moscow 125315, Russia;2. Department of Biophysics, Faculty of Biology, Moscow State University, Moscow 119991, Russia;3. Institute for Atherosclerosis Research, Skolkovo Innovative Center, Moscow 143025, Russia;4. Katholieke Universiteit Leuven, Department of Growth and Regeneration, Campus Gasthuisberg O&N1 Herestraat 49-BUS 817, 3000 Leuven, Belgium;5. Vavilov Institute of General Genetics, Russian Academy of Sciences, Moscow 119991, Russia;1. University Grenoble Alpes, IAB, Grenoble, France;2. INSERM, IAB, Grenoble, France;3. CHU de Grenoble, IAB, Grenoble, France |
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| Abstract: | Filamin, an actin cross-linker protein, has been shown to exist in platelet. The role of this protein in the platelet has remained unclear. In this report, we show that filamin inhibits the actin-activated Mg2+ -ATPase activity of platelet myosin. The activation caused by platelet actin is inhibited by 50% at the molar ratio of filamin to actin of 1/50. Platelet tropomyosin, which we showed to enhance the ATPase activity, does not abolish the effect of filamin. The results support the view that filamin stabilizes the actin network in the resting platelet. |
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